High impact information on lwr

• Megaselia-hunchback RNAi causes hunchback-like phenotypes as observed in Drosophila, but Megaselia-bicoid RNAi causes phenotypes different from corresponding RNAi experiments in Drosophila and bicoid mutant embryos [1].
• We have found that DmUbc9 binds and conjugates Drosophila Smt3 (DmSmt3) to Dorsal [2].
• In cultured cells, DmUbc9 was found to relieve inhibition of Dorsal nuclear uptake by Cactus, allowing Dorsal to enter the nucleus and activate transcription [2].
• The lesswright mutation activates Rel-related proteins, leading to overproduction of larval hemocytes in Drosophila melanogaster [3].
• This overproduction of hemocytes is attributed to the loss of lwr function primarily in hemocytes and the lymph glands, a hematopoietic organ in Drosophila larvae [3].

Biological context of lwr

• Therefore, the lwr mutation leads to the activation of these Rel-related proteins, key transcription factors in hematopoiesis [3].
• The lwr lethal phenotype is rescued by a Drosophila UBC9/lwr transgene [4].
• The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis [5].
• A two base pair change in the most conserved region of the hunchback-like binding sequence completely abolishes protein binding [6].

Anatomical context of lwr

• Here, we demonstrate that lwr function regulates the production of blood cells (hemocytes) in Drosophila larvae. lwr mutant larvae develop many melanotic tumors in the hemolymph at the third instar stage [3].

Other interactions of lwr

• The effect of DmUbc9 on Dorsal activity was potentiated by the overexpression of DmSmt3 [2].
• Further, two-hybrid system analysis reveals DmUbc9 interaction with Drosophila and mammalian Hsp27 [7].

Analytical, diagnostic and therapeutic context of lwr

• Highly conserved during evolution, the enzyme Ubc9 activates the small ubiquitin-like modifier (SUMO) prior to its covalent ligation to target proteins [8].

References